2plv

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==Overview==
==Overview==
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The three-dimensional structure of the Sabin strain of type 3 poliovirus, has been determined at 2.4 A resolution. Significant structural, differences with the Mahoney strain of type 1 poliovirus are confined to, loops and terminal extensions of the capsid proteins, occur in all of the, major antigenic sites of the virion and typically involve insertions, deletions or the replacement of prolines. Several newly identified, components of the structure participate in assembly-dependent interactions, which are relevant to the biologically important processes of viral, assembly and uncoating. These include two sites of lipid substitution, two, putative nucleotides and a beta sheet formed by the N-termini of capsid, proteins VP4 and VP1. The structure provides an explanation for the, temperature sensitive phenotype of the P3/Sabin strain. Amino acids that, regulate temperature sensitivity in type 3 poliovirus are located in the, interfaces between promoters, in the binding site for a lipid substituent, and in an assembly-dependent extended beta sheet that stabilizes the, association of pentamers. Several lines of evidence indicate that these, structural components also control conformational transitions at various, stages of the viral life cycle.
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The three-dimensional structure of the Sabin strain of type 3 poliovirus has been determined at 2.4 A resolution. Significant structural differences with the Mahoney strain of type 1 poliovirus are confined to loops and terminal extensions of the capsid proteins, occur in all of the major antigenic sites of the virion and typically involve insertions, deletions or the replacement of prolines. Several newly identified components of the structure participate in assembly-dependent interactions which are relevant to the biologically important processes of viral assembly and uncoating. These include two sites of lipid substitution, two putative nucleotides and a beta sheet formed by the N-termini of capsid proteins VP4 and VP1. The structure provides an explanation for the temperature sensitive phenotype of the P3/Sabin strain. Amino acids that regulate temperature sensitivity in type 3 poliovirus are located in the interfaces between promoters, in the binding site for a lipid substituent and in an assembly-dependent extended beta sheet that stabilizes the association of pentamers. Several lines of evidence indicate that these structural components also control conformational transitions at various stages of the viral life cycle.
==About this Structure==
==About this Structure==
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[[Category: Poliovirus and Rhinovirus]]
[[Category: Poliovirus and Rhinovirus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Filman, D.J.]]
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[[Category: Filman, D J.]]
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[[Category: Hogle, J.M.]]
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[[Category: Hogle, J M.]]
[[Category: MYR]]
[[Category: MYR]]
[[Category: SPH]]
[[Category: SPH]]
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[[Category: picornavirus]]
[[Category: picornavirus]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:41:48 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:30:56 2008''

Revision as of 16:30, 21 February 2008


2plv, resolution 2.88Å

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STRUCTURAL FACTORS THAT CONTROL CONFORMATIONAL TRANSITIONS AND SEROTYPE SPECIFICITY IN TYPE 3 POLIOVIRUS

Overview

The three-dimensional structure of the Sabin strain of type 3 poliovirus has been determined at 2.4 A resolution. Significant structural differences with the Mahoney strain of type 1 poliovirus are confined to loops and terminal extensions of the capsid proteins, occur in all of the major antigenic sites of the virion and typically involve insertions, deletions or the replacement of prolines. Several newly identified components of the structure participate in assembly-dependent interactions which are relevant to the biologically important processes of viral assembly and uncoating. These include two sites of lipid substitution, two putative nucleotides and a beta sheet formed by the N-termini of capsid proteins VP4 and VP1. The structure provides an explanation for the temperature sensitive phenotype of the P3/Sabin strain. Amino acids that regulate temperature sensitivity in type 3 poliovirus are located in the interfaces between promoters, in the binding site for a lipid substituent and in an assembly-dependent extended beta sheet that stabilizes the association of pentamers. Several lines of evidence indicate that these structural components also control conformational transitions at various stages of the viral life cycle.

About this Structure

2PLV is a Protein complex structure of sequences from Human poliovirus 1 with and as ligands. The following page contains interesting information on the relation of 2PLV with [Poliovirus and Rhinovirus]. Full crystallographic information is available from OCA.

Reference

Structural factors that control conformational transitions and serotype specificity in type 3 poliovirus., Filman DJ, Syed R, Chow M, Macadam AJ, Minor PD, Hogle JM, EMBO J. 1989 May;8(5):1567-79. PMID:2548847

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